Recombinant Human FBN3 protein

Fibrillin-3 (FBN3) is a member of the fibrillin family of extracellular matrix glycoproteins, which includes FBN1 and FBN2. These proteins are essential for forming microfibrils that provide structural support to tissues and regulate growth factor signaling, particularly TGF-β. While FBN1 mutations are linked to Marfan syndrome and FBN2 to congenital contractural arachnodactyly, FBN3 remains less characterized. It is primarily expressed during embryonic development, suggesting a role in early tissue formation, though its postnatal functions are poorly understood.

Recombinant FBN3 protein refers to the engineered form produced in vitro using expression systems like mammalian cells or bacteria. This allows researchers to study its structure, interactions, and mechanisms without relying on native tissue sources. The recombinant protein retains key domains, including calcium-binding epidermal growth factor (cbEGF)-like motifs and TGF-β-binding regions, enabling investigations into its potential roles in cell adhesion, matrix assembly, or developmental pathways.

Interest in FBN3 has grown due to its speculated involvement in diseases. Some studies associate altered FBN3 expression with cancers or metabolic disorders, though evidence remains preliminary. Its restricted developmental expression also raises questions about reactivation in pathological conditions. Recombinant FBN3 tools aid in exploring these hypotheses, including antibody development, binding assays, or disease modeling. However, challenges persist in clarifying its distinct functions compared to other fibrillins and translating findings into clinical applications. Current research focuses on mapping its interactome, epigenetic regulation, and potential as a biomarker or therapeutic target.